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Structural insights into the intermolecular interaction of the adhesin SdrC in the pathogenicity of Staphylococcus aureus
Acta Crystallographica Section F ( IF 1.072 ) Pub Date : 2021-02-23 , DOI: 10.1107/s2053230x21000741
Junchao Wang 1 , Min Zhang 1 , Mingzhu Wang 2 , Jianye Zang 3 , Xuan Zhang 3 , Tianrong Hang 1
Affiliation  

Staphylococcus aureus is an opportunistic disease‐causing pathogen that is widely found in the community and on medical equipment. A series of virulence factors secreted by S. aureus can trigger severe diseases such as sepsis, endocarditis and toxic shock, and thus have a great impact on human health. The transformation of S. aureus from a colonization state to a pathogenic state during its life cycle is intimately associated with the initiation of bacterial aggregation and biofilm accumulation. SdrC, an S. aureus surface protein, can act as an adhesin to promote cell attachment and aggregation by an unknown mechanism. Here, structural studies demonstrate that SdrC forms a unique dimer through intermolecular interaction. It is proposed that the dimerization of SdrC enhances the efficiency of bacteria–host attachment and therefore contributes to the pathogenicity of S. aureus.

中文翻译:

粘附素 SdrC 在金黄色葡萄球菌致病性中分子间相互作用的结构见解

金黄色葡萄球菌是一种机会性致病病原体,广泛存在于社区和医疗设备上。金黄色葡萄球菌分泌的一系列毒力因子可引发败血症、心内膜炎、中毒性休克等严重疾病,从而对人类健康产生重大影响。金黄色葡萄球菌在其生命周期中从定植状态转变为致病状态与细菌聚集和生物膜积累的开始密切相关。SdrC,一种金黄色葡萄球菌表面蛋白,可以作为粘附素通过未知机制促进细胞附着和聚集。在这里,结构研究表明 SdrC 通过分子间相互作用形成独特的二聚体。有人提出,SdrC 的二聚化提高了细菌-宿主附着的效率,因此有助于金黄色葡萄球菌的致病性。
更新日期:2021-02-23
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